ID DGK2_LACAC Reviewed; 228 AA.
AC P0C1G0; Q59484; Q5FHS9;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Deoxyguanosine kinase;
DE Short=DGK;
DE Short=DGUO kinase;
DE EC=2.7.1.113;
DE AltName: Full=Deoxynucleoside kinase complex I F-component;
GN OrderedLocusNames=LBA1950;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
CC -!- FUNCTION: DGK/DAK plays an essential role in generating the
CC deoxyribonucleotide precursors, dGTP and dATP, for DNA metabolism.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+);
CC Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216;
CC EC=2.7.1.113;
CC -!- SUBUNIT: Heterodimer of a deoxyadenosine (DAK) and a deoxyguanosine
CC kinase (DGK). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; CP000033; AAV43745.1; -; Genomic_DNA.
DR RefSeq; WP_003549464.1; NC_006814.3.
DR RefSeq; YP_194776.1; NC_006814.3.
DR AlphaFoldDB; P0C1G0; -.
DR SMR; P0C1G0; -.
DR STRING; 272621.LBA1950; -.
DR GeneID; 56943497; -.
DR KEGG; lac:LBA1950; -.
DR PATRIC; fig|272621.13.peg.1854; -.
DR eggNOG; COG1428; Bacteria.
DR HOGENOM; CLU_030466_2_1_9; -.
DR OrthoDB; 9776634at2; -.
DR BioCyc; LACI272621:G1G49-1901-MONOMER; -.
DR Proteomes; UP000006381; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10513; DEOXYNUCLEOSIDE KINASE; 1.
DR PANTHER; PTHR10513:SF15; NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 10, MITOCHONDRIAL; 1.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..228
FT /note="Deoxyguanosine kinase"
FT /id="PRO_0000175096"
FT ACT_SITE 78
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 8..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 32
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 44
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 228 AA; 26691 MW; 6AD4F19B283B6C37 CRC64;
MTVIVLSGPI GAGKSSLTGI LSKYLGTKPF YESVDDNPVL PLFYADPKKY AFLLQVYFLN
TRFHSIKNAL TQDNNVLDRS IYEDALFFQM NADIGRATSE EVDTYYELLH NMMGELDRMP
KKNPDLLVHI NVSYDTMIKR IKKRGRPYEQ LSYDSTLEDY YKRLLRYYKP WYEKYDYSPK
MVIDGDKYDF MSSEADREIV LDQIVDKLKE VGKLPMDWDK STDIQIEA
//
